ID   B2ABI8_PODAN            Unreviewed;       894 AA.
AC   B2ABI8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|EMBL:CDP24473.1};
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 5 {ECO:0000313|EMBL:CAP60810.1};
GN   ORFNames=PODANS_1_20820 {ECO:0000313|EMBL:CAP60810.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP60810.1};
RN   [1] {ECO:0000313|EMBL:CAP60810.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP60810.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP60810.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP60810.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP24473.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CU633445; CAP60810.1; -; Genomic_DNA.
DR   EMBL; FO904936; CDP24473.1; -; Genomic_DNA.
DR   RefSeq; XP_001903038.1; XM_001903003.1.
DR   AlphaFoldDB; B2ABI8; -.
DR   STRING; 515849.B2ABI8; -.
DR   GeneID; 6187157; -.
DR   KEGG; pan:PODANSg050; -.
DR   VEuPathDB; FungiDB:PODANS_1_20820; -.
DR   eggNOG; KOG1083; Eukaryota.
DR   HOGENOM; CLU_004379_1_0_1; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000001197; Chromosome 1.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR22884:SF512; N-METHYLTRANSFERASE (ASH1), PUTATIVE (AFU_ORTHOLOGUE AFUA_3G06480)-RELATED; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          435..482
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          493..609
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          617..633
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          31..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..657
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  95293 MW;  8572DDC28D142C0A CRC64;
     MATDMAATIA TDVATSSIAA GLGCVIMSES SFSATPTDDS SNAASLSSTP PTTCTPDSMS
     LASEPDATKP ASMADATIEA VIPILENEAA ADDNQQQQQP GELSPVGQAI VVAEPLPSTE
     SLSTGRPRRA RASLPVYNLS QLSGTDKRRR RVAGQGVQEN RRRTIAGDAG GEADANRSTG
     IDVLALGGSV SGTSTPKGAR ISSKTKPIPV QAPIVTRRAT RQSGAPVETL ATKVAALGRK
     GRKSAQSLGR ISRELMRLQD TNEFAHIDTR PVKYTVWSNG KYVDVDPAAE PPRKKTKVDG
     KPKTETSKER ATTEPSEPVR PPVKQRRVKQ WHRKGLYAGQ ETPTDITQGL TTQEKKQLAQ
     IPELLKPVKA NKTLPLPMYN GLRMLIHGRD FKLPFDVCNP LPPGQPKPPA YRTIAKNRFV
     GDAAAYWKKS PHFEDFSSKC VCKPEDGCAE DCQNRIMLYE CDDTNCNAGR EFCQNRAFQD
     LQERTKKGGR FRVGVEVLKT SDRGYGVRST RCFEPNQIIM EYTGEIITEE ECERRMNEKY
     KDNECYYLMS FDQNMIIDAT TGSMARFVNH SCSPNCRMIK WIVSGQPRMA LFAGDKPIMT
     GDELTYDYNF DPFSAKNVQK CLCGSANCRG VLGPKPKEVK PPKPAKQEKK TARGSIKAGK
     RKLKELLVGA EDEASGGNAA KKRKVQPAAG VKKTLTAAAK GAAKTAAAKG KGLARGVSKS
     ASTAIKRSVS GTISLGASAL KSTKGAGVKK TTTTTQRKVT SVGLTKTFGK RGVKTTTTTT
     TKIKLSAKST SSKATIVAAG PKPTPKKPAA GAKASTPASA SASAASARKR TPSRKALEAS
     TPDAGNTSVK GTSASSDVKA KVTTTTTTTA AVKLKQTKIK FVPKANAVAA AAAE
//